Evidence map›Paper›PMID 34157114›Full record

ArticleNucleic acids research2021

Rrp1 translocase and ubiquitin ligase activities restrict the genome destabilising effects of Rad51 in fission yeast.

Jakub Muraszko, Karol Kramarz, Bilge Argunhan, Kentaro Ito, Gabriela Baranowska, Yumiko Kurokawa, Yasuto Murayama, Hideo Tsubouchi, Sarah Lambert, Hiroshi Iwasaki and 1 more

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.6field-weighted citation impact, top 36% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

6 citing papers in PubMed, 10 citations in OpenAlex.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

11 authors at 3 institutions in 3 countries.

Jakub MuraszkoFaculty of Biotechnology, University of Wrocław, Poland.
Karol KramarzInstitut Curie, Université PSL, CNRS UMR3348, 91400 Orsay, France.
Bilge ArgunhanCell Biology Center, Institute of Innovative Research, Tokyo Institute of Technology, Japan.
Kentaro ItoCell Biology Center, Institute of Innovative Research, Tokyo Institute of Technology, Japan.
Gabriela BaranowskaFaculty of Biotechnology, University of Wrocław, Poland.
Yumiko KurokawaCell Biology Center, Institute of Innovative Research, Tokyo Institute of Technology, Japan.
Yasuto MurayamaCell Biology Center, Institute of Innovative Research, Tokyo Institute of Technology, Japan.
Hideo TsubouchiCell Biology Center, Institute of Innovative Research, Tokyo Institute of Technology, Japan.
Sarah LambertInstitut Curie, Université PSL, CNRS UMR3348, 91400 Orsay, France.
Hiroshi IwasakiCell Biology Center, Institute of Innovative Research, Tokyo Institute of Technology, Japan.ORCID 0000-0002-0153-6873
Dorota DziadkowiecFaculty of Biotechnology, University of Wrocław, Poland.ORCID 0000-0003-0912-2111
Tokyo Institute of Technology · JPUniversity of Wrocław · PLCentre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Rad51 is the key protein in homologous recombination that plays important roles during DNA replication and repair. Auxiliary factors regulate Rad51 activity to facilitate productive recombination, and prevent inappropriate, untimely or excessive events, which could lead to genome instability. Previous genetic analyses identified a function for Rrp1 (a member of the Rad5/16-like group of SWI2/SNF2 translocases) in modulating Rad51 function, shared with the Rad51 mediator Swi5-Sfr1 and the Srs2 anti-recombinase. Here, we show that Rrp1 overproduction alleviates the toxicity associated with excessive Rad51 levels in a manner dependent on Rrp1 ATPase domain. Purified Rrp1 binds to DNA and has a DNA-dependent ATPase activity. Importantly, Rrp1 directly interacts with Rad51 and removes it from double-stranded DNA, confirming that Rrp1 is a translocase capable of modulating Rad51 function. Rrp1 affects Rad51 binding at centromeres. Additionally, we demonstrate in vivo and in vitro that Rrp1 possesses E3 ubiquitin ligase activity with Rad51 as a substrate, suggesting that Rrp1 regulates Rad51 in a multi-tiered fashion.

Indexed as

Adenosine TriphosphatasesDNA-Binding ProteinsDNA, FungalGenomic InstabilityRad51 RecombinaseSchizosaccharomycesSchizosaccharomyces pombe ProteinsUbiquitin-Protein LigasesAdenosine TriphosphatasesDNA-Binding ProteinsDNA, FungalRad51 RecombinaseRHP51 protein, S pombeRrp1 protein, S pombeRrp2 protein, S pombeSchizosaccharomyces pombe ProteinsUbiquitin-Protein Ligases

Identifiers

PMID34157114
PMCPMC8266636
OpenAlexW3173348800

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.